Evidence map›Paper›PMID 26044710›Full record

ArticleNucleic acids research2015

A cis-encoded sRNA, Hfq and mRNA secondary structure act independently to suppress IS200 transposition.

Michael J Ellis, Ryan S Trussler, David B Haniford

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

  1. Article
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  6. Review
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  8. Article
  9. The RNA chaperone Hfq has a multifaceted role inFrontiers in cellular and infection microbiology · 2024
    Article
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  11. Article
  12. Review
  13. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Michael J EllisDepartment of Biochemistry, University of Western Ontario, London, ON, N6A 5C1, Canada.
Ryan S TrusslerDepartment of Biochemistry, University of Western Ontario, London, ON, N6A 5C1, Canada.
David B HanifordDepartment of Biochemistry, University of Western Ontario, London, ON, N6A 5C1, Canada haniford@uwo.ca.

Funding

Canadian Institutes of Health Research MOP 11281
6 · The paper itself

Abstract

IS200 is found throughout Enterobacteriaceae and transposes at a notoriously low frequency. In addition to the transposase protein (TnpA), IS200 encodes an uncharacterized Hfq-binding sRNA that is encoded opposite to the tnpA 5'UTR. In the current work we asked if this sRNA represses tnpA expression. We show here that the IS200 sRNA (named art200 for antisense regulator of transposase IS200) basepairs with tnpA to inhibit translation initiation. Unexpectedly, art200-tnpA pairing is limited to 40 bp, despite 90 nt of perfect complementarity. Additionally, we show that Hfq and RNA secondary structure in the tnpA 5'UTR each repress tnpA expression in an art200-independent manner. Finally, we show that disrupting translational control of tnpA expression leads to increased IS200 transposition in E. coli. The current work provides new mechanistic insight into why IS200 transposition is so strongly suppressed. The possibility of art200 acting in trans to regulate a yet-unidentified target is discussed as well as potential applications of the IS200 system for designing novel riboregulators.

Indexed as

DNA Transposable ElementsGene Expression Regulation, BacterialProtein BiosynthesisEscherichia coliEscherichia coli ProteinsHost Factor 1 ProteinNucleic Acid ConformationRibosome Subunits, Small, BacterialRNA, AntisenseRNA, MessengerTransposasesDNA Transposable ElementsEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinRNA, AntisenseRNA, MessengerTnpA(rep) protein, E coliTransposases

Identifiers

PMID26044710
PMCPMC4513863

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.